ID B4UYL0_9ACTN Unreviewed; 847 AA.
AC B4UYL0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=M444_01455 {ECO:0000313|EMBL:AKL64323.1}, SSAG_00141
GN {ECO:0000313|EMBL:EDX20350.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX20350.1, ECO:0000313|Proteomes:UP000005764};
RN [1] {ECO:0000313|EMBL:EDX20350.1, ECO:0000313|Proteomes:UP000005764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX20350.1,
RC ECO:0000313|Proteomes:UP000005764};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., Straight P.,
RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA Lander E., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. Mg1.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKL64323.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL64323.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
RN [3] {ECO:0000313|EMBL:AKL64323.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL64323.1};
RA Hoefler B.C., Straight P.D.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011664; AKL64323.1; -; Genomic_DNA.
DR EMBL; DS570384; EDX20350.1; -; Genomic_DNA.
DR RefSeq; WP_008734579.1; NZ_DS570384.1.
DR AlphaFoldDB; B4UYL0; -.
DR STRING; 465541.M444_01455; -.
DR KEGG; strm:M444_01455; -.
DR PATRIC; fig|465541.12.peg.368; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_1_11; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000005764; Unassembled WGS sequence.
DR Proteomes; UP000035653; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AKL64323.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 380..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..832
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 847 AA; 91084 MW; ACD9DB083F4E6CCE CRC64;
MGRGKLRIYL GAAPGVGKTY AMLSEAHRRI ERGTDCVVGF VEHHNRPRTE VMLHGLELIE
RRELEYRDAT FTEMDVDAIL ARQPAVALVD ELAHTNVPGS RNAKRWQDVE ELLQAGIDVV
STVNIQHLES LGDVVETITG VRQRETVPDE VARRADQIEL VDMSPQALRR RMAHGNVYKP
DKVDAALSNY FRPGNLTALR ELALLWVADR VDEYLQEYRG EHNIRSTWQA RERIVVGLTG
GPEGRTLIRR AARLAEKGAG GEVLAVYIAA SDGLTSASPK ELAVQRTLVE DLGGTFHHVI
GDSIPDALLE FARGCNATQI VLGVSRRRSW QYAFSPGVSA TVARESGPDL DVHIVTHDEA
AKGRRLPVAR GARLGRSRII WGWLAGIAGP ALLTVLLSQV VPELGLANDM LLFLTFTVAA
ALLGGLLPAL ASAAFGSLLL NYYFTPPLHE FTISDPLNIV AIAIFVGVAV SVASVVDLAA
RRTHQAARLR AESEILSFLA GSVLRGENSL DALLERLRET FAMQSVTLLE RTSDVDPWTT
AASVGTSPVG RPEDADVDLP IGDHMALALT GRVLPAEDRR VLGAFAAQAA VVLDRQRLVD
EAEKSRELAE ANRIRTALLA AVSHDLRTPL AGIKASVSSL RSDDVEWSED DKAELLEGIE
DGADRLAALI GNLLDMSRLN TGTVVPLIRE TDLDEVVPMA LGGVPEDSVD LDIPETLPMI
AVDRGLLERA VANIVENAVK YSPDGQPVNV TASALHERVE LRVVDRGPGV PDEAKHRIFE
PFQRHGDAPR GAGVGLGLAV ARGFTEAIGG TLTAEDTPGG GLTMVITLPI AGGAPPVTAD
LPTSAVT
//
